KEGG   ENZYME: 1.14.20.15
Entry
EC 1.14.20.15               Enzyme                                 
Name
L-threonyl-[L-threonyl-carrier protein] 4-chlorinase;
syrB2 (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and the other dehydrogenated
Sysname
L-threonyl-[L-threonyl-carrier protein],2-oxoglutarate:oxygen oxidoreductase (4-halogenating)
Reaction(IUBMB)
an L-threonyl-[L-threonyl-carrier protein] + 2-oxoglutarate + O2 + Cl- = a 4-chloro-L-threonyl-[L-threonyl-carrier protein] + succinate + CO2 + H2O [RN:R12176]
Reaction(KEGG)
R12176
Substrate
L-threonyl-[L-threonyl-carrier protein] [CPD:C21976];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007];
Cl- [CPD:C00698]
Product
4-chloro-L-threonyl-[L-threonyl-carrier protein] [CPD:C21977];
succinate [CPD:C00042];
CO2 [CPD:C00011];
H2O [CPD:C00001]
Comment
The enzyme, characterized from the bacterium Pseudomonas syringae, participates in syringomycin E biosynthesis. The enzyme is a specialized iron(II)/2-oxoglutarate-dependent oxygenase that catalyses the chlorination of its substrate in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
History
EC 1.14.20.15 created 2018
Reference
1  [PMID:16002467]
  Authors
Vaillancourt FH, Yin J, Walsh CT
  Title
SyrB2 in syringomycin E biosynthesis is a nonheme FeII alpha-ketoglutarate- and O2-dependent halogenase.
  Journal
Proc Natl Acad Sci U S A 102:10111-6 (2005)
DOI:10.1073/pnas.0504412102
Other DBs
ExplorEnz - The Enzyme Database: 1.14.20.15
IUBMB Enzyme Nomenclature: 1.14.20.15
ExPASy - ENZYME nomenclature database: 1.14.20.15
BRENDA, the Enzyme Database: 1.14.20.15

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Chemical substance (8)   
   KEGG COMPOUND (8)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
Protein sequence (101)   
   UniProt (2)   
   SWISS-PROT (1)   
   RefSeq(pep) (98)   
DNA sequence (701)   
   RefSeq(nuc) (696)   
   GenBank (3)   
   EMBL (2)   
Protein domain (2)   
   InterPro (2)   
All databases (814)   

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